Feeding strategies of methanol and lipase on eversa® transform‐mediated hydroesterification for FAME production

Abstract

This work reports the influence of different feeding strategies of methanol and catalysts on fatty acid methyl esters (FAME) yield in a beef tallow hydroesterification reaction for biodiesel production catalyzed by liquid lipase. Soluble lipase from the Thermomyces lanuginosus microorganism, named Eversa 1 Transform, was selected for the reactions in this work. The feeding of methanol and lipase into the system was evaluated varying the methanol to fat molar ratio of 4.0:1 and 4.5:1 and the lipase load of 1.0 wt% and 1.45 wt% in relation to the mass of beef tallow utilized in each assay. The highest yield (85.08 %) of FAME was reached at 35 8C, methanol to fat molar ratio of 4.5:1, 1.0 wt% of lipase, 6.0 wt% of water in only 8 h of reaction, with a one-step addition of lipase and methanol fed to the process at a constant flow of 3.0 g Á h À1 . Moreover, the reutilization process of the liquid lipase after four cycles was evaluated, which is a point rarely addressed in similar works available in the open literature. The findings of this paper demonstrate that the adoption of an appropriate strategy to feed inputs to the system is fundamental in order to take advantage of the maximum catalytic capacity of the lipase and consequently to obtain high yields in the process.

Lipases in liquid formulation for biodiesel production: Current status and challenges

“…Despite the favorable points, the enzymatic technology also presents problems/complications that must be considered: high cost of the biocatalysts in comparison with the alkaline ones; lower reaction rates, implying in higher reaction time required to achieve satisfactory conversions; and loss of catalytic activity when the lipase is under high temperatures and mainly by the denaturing action of the main reagent used in the reaction, the methanol [86,87]. In a transesterification, at least the stoichiometric amount of 3 mol of alcohol for each mole of substrate is required to complete the conversion of the TAG of the feedstock to their corresponding FAAE, whereby an excess of alcohol is usually used in order to shift the reaction equilibrium toward the products.…”

“…An interesting point to note is that as is possible for immobilized enzymes, soluble lipases also enable their reuse after recovery from the reaction medium by simple decantation [87,107,111]. The enzyme being an amphiphilic molecule acting on the interface water/oil, remains concentrated, after separation by gravity, in an emulsion between a superior layer (rich in FAAE) and a clear inferior layer (rich in glycerol and water).…”

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

“…Although many researches used immobilized lipases for hydroesterification, recently, the use of liquid lipases has gained popularity [235,[264][265][266]. The use of a liquid lipase instead of an immobilized lipase implies the presence of water in the process, thus, related to the first hydrolytic step.…”

“…The use of a liquid lipase instead of an immobilized lipase implies the presence of water in the process, thus, related to the first hydrolytic step. Moreover, water promotes alcohol dilution in the medium, reducing its denaturing effect on the enzyme and leading to the formation of a second liquid phase in the reaction, creating a hydrophobic interface that is known to activate many lipases [235,[264][265][266].…”

Immobilization of Eversa Lipases on Hydrophobic Supports for Production of Oleate Esters Solvent-Free

“…Most of the published studies about Eversa lipases are transesteri cation of triglycerides or esteri cation of free fatty acids and used these enzymes in the free form [8][9][10][11][12]. Even though Eversa enzymes may be used in free form, their immobilization may enhance many properties such as stability and resistance to inhibitors chemicals [13].…”